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Sodium-transport NADH-quinone reductase of a marineVibrio alginolyticus

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Abstract

The respiratory chain of a marine bacterium,Vibrio alginolyticus, required Na+ for maximum activity, and the site of Na+-dependent activation was localized on the NADH-quinone reductase segment. The Na+-dependent NADH-quinone reductase extruded Na+ as a direct result of redox reaction. It was composed of three subunits, α, β, and γ, with apparentMr of 52, 46, and 32 KDa, respectively. The reduction of ubiquinone-1 to ubiquinol proceeded via ubisemiquinone radicals. The former reaction was catalyzed by the FAD-containing β subunit. This reaction showed no specific requirement for Na+. For the formation of ubiquinol, the presence of the γ subunit and the FMN-containing α subunit was essential. The latter reaction specifically required Na+ for activity and was strongly inhibited by 2-n-heptyl-4-hydroxyquinolineN-oxide. It was assigned to the coupling site for Na+ transport. The mode of energy coupling of redox-driven Na+ pump was compared with those of decarboxylase- and ATP-driven Na+ pumps found in other bacteria.

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References

  • Dibrov, P. A., Kostyrko, V. A., Lazarova, R. L., Skulachev, V. P., and Smirnova, I. A. (1986a).Biochim. Biophys. Acta 850, 449–457.

    Google Scholar 

  • Dibrov, P. A., Lazarova, R. L., Skulachev, V. P., and Verkhovskaya, M. L. (1986b).Biochim. Biophys. Acta 850, 458–465.

    Google Scholar 

  • Dimroth, P. (1987).Microbiol. Rev. 51, 320–340.

    Google Scholar 

  • Dimroth, P., and Thomer, A. (1983).Eur. J. Biochem. 137, 107–112.

    Google Scholar 

  • Drapeau, G. R., and MacLeod, R. A. (1963).Biochem. Biophys. Res. Commun. 12, 111–115.

    Google Scholar 

  • Drapeau, G. R., Matula, T. I., and MacLeod, R. A. (1966).J. Bacteriol. 92, 63–71.

    Google Scholar 

  • Hayashi, M., and Unemoto, T. (1984).Biochim. Biophys. Acta 767, 470–478.

    Google Scholar 

  • Hayashi, M., and Unemoto, T. (1986).FEBS Lett. 202, 327–330.

    Google Scholar 

  • Hayashi, M., and Unemoto, T. (1987a).Biochim. Biophys. Acta 890, 47–54.

    Google Scholar 

  • Hayashi, M., and Unemoto, T. (1987b).Biochem. (Life Sci. Adv.)6, 157–161.

    Google Scholar 

  • Ken-Dror, S., Shnaiderman, R., and Avi-Dor, Y. (1984).Arch. Biochem. Biophys. 229, 640–649.

    Google Scholar 

  • Ken-Dror, S., Preger, R., and Avi-Dor, Y. (1986a).Arch. Biochem. Biophys. 244, 122–127.

    Google Scholar 

  • Ken-Dror, S., Lanyi, J. K., Schobert, B., Silver, B., and Avi-Dor, Y. (1986b).Arch. Biochem. Biophys. 244, 766–772.

    Google Scholar 

  • Khanna, G., Devoe, L., Brown, L., Niven, D. F., and MacLeod, R. A. (1984).J. Bacteriol. 157, 59–63.

    Google Scholar 

  • Kitada, M., and Horikoshi, K. (1977).J. Bacteriol. 131, 784–788.

    Google Scholar 

  • Kröger, A., and Dadák, V. (1969).Eur. J. Biochem. 11, 328–340.

    Google Scholar 

  • Krulwich, T. A. (1986).J. Membr. Biol. 89, 113–125.

    Google Scholar 

  • Kushner, D. J. (1978). InMicrobial Life in Extreme Environment (Kushner, D. J., ed.), Academic Press, London, pp. 317–368.

    Google Scholar 

  • Lanyi, J. K. (1979).Biochim. Biophys. Acta 559, 377–397.

    Google Scholar 

  • Lanyi, J. K., and Weber, H. J. (1980).J. Biol. Chem. 255, 243–250.

    Google Scholar 

  • Laubinger, W., and Dimroth, P. (1987).Eur. J. Biochem. 168, 475–480.

    Google Scholar 

  • Lewis, R. J., Belkina, S., and Krulwich, T. A. (1980).Biochem. Biophys. Res. Commun. 95, 857–863.

    Google Scholar 

  • MacLeod, R. A. (1965).Bacteriol. Rev. 29, 9–23.

    Google Scholar 

  • MacLeod, R. A., and Hori, A. (1960).J. Bacteriol. 80, 464–471.

    Google Scholar 

  • MacLeod, R. A., Claridge, C. A., Hori, A., and Murray, J. F. (1958).J. Biol. Chem. 232, 829–834.

    Google Scholar 

  • Nakamura, T., Tokuda, H., and Unemoto, T. (1982).Biochim. Biophys. Acta 692, 389–396.

    Google Scholar 

  • Niven, D. F., and MacLeod, R. A. (1978).J. Bacteriol. 134, 737–743.

    Google Scholar 

  • Niven, D. F., and MacLeod, R. A. (1980).J. Bacteriol. 142, 603–607.

    Google Scholar 

  • Ragan, C. I. (1987).Curr. Top. Bioenerg. 15, 1–36.

    Google Scholar 

  • Reichelt, J. L., and Baumann, P. (1974).Arch. Microbiol. 97, 329–345.

    Google Scholar 

  • Schobert, B., and Lanyi, J. K. (1982).J. Biol. Chem. 257, 10306–10313.

    Google Scholar 

  • Skulachev, V. P. (1987). InIon Transport in Prokaryotes (Rosen, B. P., and Silver, S., eds.), Academic Press, London, pp. 131–164.

    Google Scholar 

  • Sprott, G. D., and MacLeod, R. A. (1974).J. Bacteriol. 117, 1043–1054.

    Google Scholar 

  • Szarkowska, L., and Klingenberg, M. (1963).Biochem. Z. 338, 674–697.

    Google Scholar 

  • Takada, Y., Fukunaga, N., and Sasaki, S. (1981).J. Gen. Appl. Microbiol. 27, 327–337.

    Google Scholar 

  • Takada, Y., Fukunaga, N., and Sasaki, S. (1988).Plant Cell Physiol. 29, 207–214.

    Google Scholar 

  • Thompson, J., and MacLeod, R. A. (1974).J. Bacteriol. 117, 1055–1064.

    Google Scholar 

  • Tokuda, H. (1983).Biochem. Biophys. Res. Commun. 114, 113–118.

    Google Scholar 

  • Tokuda, H., and Unemoto, T. (1981).Biochem. Biophys. Res. Commun. 102, 265–271.

    Google Scholar 

  • Tokuda, H., and Unemoto, T. (1982).J. Biol. Chem. 257, 10007–10014.

    Google Scholar 

  • Tokuda, H., and Unemoto, T. (1983).J. Bacteriol. 156, 636–643.

    Google Scholar 

  • Tokuda, H., and Unemoto, T. (1984).J. Biol. Chem. 259, 7785–7790.

    Google Scholar 

  • Tokuda, H., Sugasawa, M., and Unemoto, T. (1982).J. Biol. Chem. 257, 788–794.

    Google Scholar 

  • Tomlinson, N., and MacLeod, R. A. (1957).Can. J. Microbiol. 3, 627–638.

    Google Scholar 

  • Tsuchiya, T., and Shinoda, S. (1985).J. Bacteriol. 162, 794–798.

    Google Scholar 

  • Udagawa, T., Unemoto, T., and Tokuda, H. (1986).J. Biol. Chem. 261, 2616–2622.

    Google Scholar 

  • Unemoto, T., and Hayashi, M. (1979).J. Biochem. 85, 1461–1467.

    Google Scholar 

  • Unemoto, T., Tsuruoka, T., and Hayashi, M. (1973).Can. J. Microbiol. 19, 563–571.

    Google Scholar 

  • Unemoto, T., Hayashi, M., Kozuka, Y., and Hayashi, M. (1974). InEffect of the Ocean Environment on Microbial Activities (Colwell, R. R., and Morita, R. Y., eds.), University Park Press, Baltimore, pp. 46–71.

    Google Scholar 

  • Unemoto, T., Hayashi, M., and Hayashi, M. (1977).J. Biochem. 82, 1389–1395.

    Google Scholar 

  • Unemoto, T., Hayashi, M., and Hayashi, M. (1981).J. Biochem. 90, 619–628.

    Google Scholar 

  • Watanabe, H., Takimoto, A., and Nakamura, T. (1977).J. Biochem. 82, 1707–1714.

    Google Scholar 

  • Wikström, M., and Krab, K. (1980).Curr. Top. Bioenerg. 10, 51–101.

    Google Scholar 

  • Wong, P. T. S., Thompson, J., and MacLeod, R. A. (1969).J. Biol. Chem. 244, 1016–1025.

    Google Scholar 

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  1. Laboratory of Membrane Biochemistry, Faculty of Pharmaceutical Sciences, Chiba University, 1-33, Yayoi-cho, 260, Chiba, Japan

    Tsutomu Unemoto & Maki Hayashi

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  1. Tsutomu Unemoto
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  2. Maki Hayashi
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Unemoto, T., Hayashi, M. Sodium-transport NADH-quinone reductase of a marineVibrio alginolyticus . J Bioenerg Biomembr 21, 649–662 (1989). https://doi.org/10.1007/BF00762684

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